2AZD

X-Ray studies on Maltodextrin Phosphorylase (MalP) Complexes: recognition of substrates and CATALYTIC mechanism of phosphorylase family

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004645	molecular_function	1,4-alpha-oligoglucan phosphorylase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0005980	biological_process	glycogen catabolic process
A	0008184	molecular_function	glycogen phosphorylase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0030980	biological_process	alpha-glucan catabolic process
A	0031220	molecular_function	maltodextrin phosphorylase activity
A	0042803	molecular_function	protein homodimerization activity
A	0102250	molecular_function	obsolete linear malto-oligosaccharide phosphorylase activity
A	0102499	molecular_function	obsolete SHG alpha-glucan phosphorylase activity
B	0004645	molecular_function	1,4-alpha-oligoglucan phosphorylase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0005980	biological_process	glycogen catabolic process
B	0008184	molecular_function	glycogen phosphorylase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0030980	biological_process	alpha-glucan catabolic process
B	0031220	molecular_function	maltodextrin phosphorylase activity
B	0042803	molecular_function	protein homodimerization activity
B	0102250	molecular_function	obsolete linear malto-oligosaccharide phosphorylase activity
B	0102499	molecular_function	obsolete SHG alpha-glucan phosphorylase activity

Functional Information from PROSITE/UniProt

site_id	PS00102
Number of Residues	13
Details	PHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtGnMKlaLN

Chain	Residue	Details
A	GLU637-ASN649

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842

Chain	Residue	Details
A	LEU251
B	LEU251

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: N6-(pyridoxal phosphate)lysine

Chain	Residue	Details
A	LEU646
B	LEU646

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1gpa

Chain	Residue	Details
A	THR641
A	LYS533
A	ARG534
A	LYS539

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1gpa

Chain	Residue	Details
B	THR641
B	LYS533
B	ARG534
B	LYS539

---